1kio: Difference between revisions
New page: left|200px<br /><applet load="1kio" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kio" /> '''SOLUTION STRUCTURE OF THE SMALL SERINE PROTE... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1kio.jpg|left|200px]]<br /><applet load="1kio" size=" | [[Image:1kio.jpg|left|200px]]<br /><applet load="1kio" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1kio" /> | caption="1kio" /> | ||
'''SOLUTION STRUCTURE OF THE SMALL SERINE PROTEASE INHIBITOR SGCI[L30R, K31M]'''<br /> | '''SOLUTION STRUCTURE OF THE SMALL SERINE PROTEASE INHIBITOR SGCI[L30R, K31M]'''<br /> | ||
==Overview== | ==Overview== | ||
The solution structure of three small serine proteinase inhibitors, two | The solution structure of three small serine proteinase inhibitors, two natural and one engineered protein, SGCI (Schistocerca gregaria chymotrypsin inhibitor), SGCI[L30R, K31M] and SGTI (Schistocerca gregaria trypsin inhibitor), were determined by homonuclear NMR-spectroscopy. The molecules exhibit different specificities towards target proteinases, where SGCI is a good chymotrypsin inhibitor, its mutant is a potent trypsin inhibitor, and SGTI inhibits both proteinases weakly. Interestingly, SGTI is a much better inhibitor of insect proteinases than of the mammalian ones used in common assays. All three molecules have a similar fold composed from three antiparallel beta-pleated sheets with three disulfide bridges. The proteinase binding loop has a somewhat distinct geometry in all three peptides. Moreover, the stabilization of the structure is different in SGCI and SGTI. Proton-deuterium exchange experiments are indicative of a highly rigid core in SGTI but not in SGCI. We suggest that the observed structural properties play a significant role in the specificity of these inhibitors. | ||
==About this Structure== | ==About this Structure== | ||
1KIO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | 1KIO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KIO OCA]. | ||
==Reference== | ==Reference== | ||
| Line 20: | Line 20: | ||
[[Category: specificity]] | [[Category: specificity]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:34:36 2008'' | ||
Revision as of 14:34, 21 February 2008
|
SOLUTION STRUCTURE OF THE SMALL SERINE PROTEASE INHIBITOR SGCI[L30R, K31M]
OverviewOverview
The solution structure of three small serine proteinase inhibitors, two natural and one engineered protein, SGCI (Schistocerca gregaria chymotrypsin inhibitor), SGCI[L30R, K31M] and SGTI (Schistocerca gregaria trypsin inhibitor), were determined by homonuclear NMR-spectroscopy. The molecules exhibit different specificities towards target proteinases, where SGCI is a good chymotrypsin inhibitor, its mutant is a potent trypsin inhibitor, and SGTI inhibits both proteinases weakly. Interestingly, SGTI is a much better inhibitor of insect proteinases than of the mammalian ones used in common assays. All three molecules have a similar fold composed from three antiparallel beta-pleated sheets with three disulfide bridges. The proteinase binding loop has a somewhat distinct geometry in all three peptides. Moreover, the stabilization of the structure is different in SGCI and SGTI. Proton-deuterium exchange experiments are indicative of a highly rigid core in SGTI but not in SGCI. We suggest that the observed structural properties play a significant role in the specificity of these inhibitors.
About this StructureAbout this Structure
1KIO is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
ReferenceReference
Comparative structure analysis of proteinase inhibitors from the desert locust, Schistocerca gregaria., Gaspari Z, Patthy A, Graf L, Perczel A, Eur J Biochem. 2002 Jan;269(2):527-37. PMID:11856311
Page seeded by OCA on Thu Feb 21 13:34:36 2008